Covalent modification of soy protein isolate by (-)-epigallocatechin-3-gallate: effects on structural and emulsifying properties

J Sci Food Agric. 2018 Dec;98(15):5683-5689. doi: 10.1002/jsfa.9114. Epub 2018 Jun 29.

Abstract

Background: Soy protein isolate (SPI) has promising applications in various food products because of its excellent functional properties and nutritional quality. The structural and emulsifying properties of covalently modified SPI by (-)-epigallocatechin-3-gallate (EGCG) were investigated.

Results: SPI was covalently modified by EGCG under alkaline conditions. SDS-PAGE analysis revealed that EGCG modification caused crosslinking of SPI proteins. Circular dichroism spectra demonstrated that the secondary structure of SPI proteins was changed by EGCG modification. In addition, the modifications resulted in the perturbation of the tertiary structure of SPI as evidenced by intrinsic fluorescence spectra and surface hydrophobicity measurements. Oil-in-water emulsions of modified SPI had smaller droplet sizes and better creaming stability compared to those from unmodified SPI.

Conclusion: The covalent modification by EGCG improved the emulsifying property of SPI. This study therefore provided an innovative approach for improving the emulsifying properties of proteins. © 2018 Society of Chemical Industry.

Keywords: (−)-Epigallocatechin-3-gallate; covalent modification; emulsifying property; soy protein isolate.

MeSH terms

  • Catechin / analogs & derivatives
  • Catechin / chemistry
  • Circular Dichroism
  • Emulsions / chemistry
  • Hydrophobic and Hydrophilic Interactions
  • Protein Conformation, alpha-Helical
  • Soybean Proteins / chemistry*
  • Soybean Proteins / isolation & purification

Substances

  • Emulsions
  • Soybean Proteins
  • Catechin
  • epigallocatechin gallate